ID A0A317B6F0_9PLEO Unreviewed; 209 AA. AC A0A317B6F0; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 24-JAN-2024, entry version 10. DE RecName: Full=deoxyhypusine synthase {ECO:0000256|ARBA:ARBA00012683}; DE EC=2.5.1.46 {ECO:0000256|ARBA:ARBA00012683}; GN ORFNames=PtrARCrB10_05718 {ECO:0000313|EMBL:PWO25732.1}; OS Pyrenophora tritici-repentis. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; OC Pyrenophora. OX NCBI_TaxID=45151 {ECO:0000313|EMBL:PWO25732.1, ECO:0000313|Proteomes:UP000245403}; RN [1] {ECO:0000313|EMBL:PWO25732.1, ECO:0000313|Proteomes:UP000245403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ARCrossB10 {ECO:0000313|EMBL:PWO25732.1, RC ECO:0000313|Proteomes:UP000245403}; RX PubMed=29685100; DOI=10.1186/s12864-018-4680-3; RA Moolhuijzen P., See P.T., Hane J.K., Shi G., Liu Z., Oliver R.P., RA Moffat C.S.; RT "Comparative genomics of the wheat fungal pathogen Pyrenophora tritici- RT repentis reveals chromosomal variations and genome plasticity."; RL BMC Genomics 19:279-279(2018). CC -!- FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine CC and the subsequent transfer of the butylamine moiety of spermidine to CC the epsilon-amino group of a specific lysine residue of the eIF-5A CC precursor protein to form the intermediate deoxyhypusine residue. CC {ECO:0000256|ARBA:ARBA00002823}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[eIF5A protein]-L-lysine + spermidine = [eIF5A protein]- CC deoxyhypusine + propane-1,3-diamine; Xref=Rhea:RHEA:33299, Rhea:RHEA- CC COMP:10143, Rhea:RHEA-COMP:10144, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57484, ChEBI:CHEBI:57834, ChEBI:CHEBI:82657; EC=2.5.1.46; CC Evidence={ECO:0000256|ARBA:ARBA00000952}; CC -!- PATHWAY: Protein modification; eIF5A hypusination. CC {ECO:0000256|ARBA:ARBA00005041}. CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family. CC {ECO:0000256|ARBA:ARBA00009892}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PWO25732.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NQWZ01000143; PWO25732.1; -; Genomic_DNA. DR AlphaFoldDB; A0A317B6F0; -. DR Proteomes; UP000245403; Unassembled WGS sequence. DR Gene3D; 3.40.910.10; Deoxyhypusine synthase; 1. DR InterPro; IPR002773; Deoxyhypusine_synthase. DR InterPro; IPR036982; Deoxyhypusine_synthase_sf. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR PANTHER; PTHR11703; DEOXYHYPUSINE SYNTHASE; 1. DR PANTHER; PTHR11703:SF0; DEOXYHYPUSINE SYNTHASE; 1. DR Pfam; PF01916; DS; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. PE 3: Inferred from homology; SQ SEQUENCE 209 AA; 23366 MW; 91A121E2A937737D CRC64; MNRIGNLVVP NSNYCAFEDW VVPILDKMLE EQEASKKTAE PLHWTPSKMI HRLGKEINDE RSVYYWAWKN DIPVFCPALT DGSLGDMLYF HTFKSSPEQL RVDIVEDIRN INTIAVRAKR TGMIVLGGGI VKHHIANANL MRNGAESAVY INTAQEFDGS DAGARPDEAV SWGKIKLDGD SVKVYAEATV VFPLIVAATF ARLQKTQDQ //